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Protein

Fusion glycoprotein F0

Gene

F

Organism
Phocine distemper virus (PDV)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).By similarity

GO - Biological processi

Keywordsi

Biological processFusion of virus membrane with host cell membrane, Fusion of virus membrane with host membrane, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Fusion glycoprotein F0
Cleaved into the following 2 chains:
Gene namesi
Name:F
OrganismiPhocine distemper virus (PDV)
Taxonomic identifieri11240 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeMorbillivirus
Virus hostiPhocidae (true seals) [TaxID: 9709]

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini11 – 483ExtracellularBy similarityAdd BLAST473
Transmembranei484 – 504HelicalSequence analysisAdd BLAST21
Topological domaini505 – 537CytoplasmicBy similarityAdd BLAST33

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 10Sequence analysis10
ChainiPRO_000003932911 – 537Fusion glycoprotein F0Add BLAST527
ChainiPRO_000003932711 – 99Fusion glycoprotein F2Add BLAST89
ChainiPRO_0000039328100 – 537Fusion glycoprotein F1Add BLAST438

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi16N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi48N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi54N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi55 ↔ 182Interchain (between F2 and F1 chains)By similarity
Disulfide bondi321 ↔ 330By similarity
Disulfide bondi345 ↔ 353By similarity
Disulfide bondi377 ↔ 382By similarity
Disulfide bondi384 ↔ 407By similarity

Post-translational modificationi

The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei99 – 100Cleavage; by hostBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP28886

Interactioni

Subunit structurei

Homotrimer of disulfide-linked F1-F2.By similarity

Structurei

3D structure databases

ProteinModelPortaliP28886
SMRiP28886
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 124Fusion peptideBy similarityAdd BLAST25

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili125 – 153Sequence analysisAdd BLAST29
Coiled coili449 – 474Sequence analysisAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi493 – 500Poly-Leu8

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiView protein in InterPro
IPR000776 Fusion_F0_Paramyxovir
PfamiView protein in Pfam
PF00523 Fusion_gly, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28886-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVILVHCVMG QIHWTNLSTI GIIGTDSSHY KIMTRSSHQY LVLKLMPNVS
60 70 80 90 100
IIDNCTKAEL DEYEKLLNSV LEPINQALTL MTKNVKSLQS LGSGRRQRRF
110 120 130 140 150
AGVVIAGAAL GVATAAQITA GVALYQSNLN AQAIQSLRAS LEQSNKAIDE
160 170 180 190 200
VRQASQNIII AVQGVQDYVN NEIVPALQHM SCELIGQRLG LKLLRYYTEL
210 220 230 240 250
LSVFGPSLRD PISAEISIQA LSYALGGEIH KILEKLGYSG NDMVAILETK
260 270 280 290 300
GIRAKITHVD LSGKFIVLSI SYPTLSEVKG VVVHRLEAVS YNIGSQEWYT
310 320 330 340 350
TVPRYVATNG YLISNFDESS CVFVSESAIC SQNSLYPMSP ILQQCLRGET
360 370 380 390 400
ASCARTLVSG TLGNKFILSK GNIIANCASI LCKCHSTSKI INQSPDKLLT
410 420 430 440 450
FIASDTCSLV EIDGVTIQVG SRQYPDVVYA SKVILGPAIS LERLDVGTNL
460 470 480 490 500
GSALKKLDDA KVLIESSDQI LDTVKNSYLS LGTLIALPVS IGLGLILLLL
510 520 530
ICCCKKRYQH LFSQSTKVAP VFKPDLTGTS KSYVRSL
Length:537
Mass (Da):58,295
Last modified:November 22, 2005 - v2
Checksum:i31097C9C6085BF7C
GO

Sequence cautioni

The sequence BAA01206 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10371 Genomic RNA Translation: BAA01206.1 Different initiation.
PIRiA48346
JQ1368 VGNZPD

Similar proteinsi

Entry informationi

Entry nameiFUS_PHODV
AccessioniPrimary (citable) accession number: P28886
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: November 22, 2005
Last modified: May 23, 2018
This is version 89 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

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